ID A0A317FG31_9PROT Unreviewed; 424 AA.
AC A0A317FG31;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:PWS36496.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:PWS36496.1};
GN ORFNames=DFH01_15210 {ECO:0000313|EMBL:PWS36496.1};
OS Falsiroseomonas bella.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Falsiroseomonas.
OX NCBI_TaxID=2184016 {ECO:0000313|EMBL:PWS36496.1, ECO:0000313|Proteomes:UP000245765};
RN [1] {ECO:0000313|Proteomes:UP000245765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQN31 {ECO:0000313|Proteomes:UP000245765};
RA Du Z., Wang X.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWS36496.1}.
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DR EMBL; QGNA01000003; PWS36496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317FG31; -.
DR OrthoDB; 9803027at2; -.
DR Proteomes; UP000245765; Unassembled WGS sequence.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd01317; DHOase_IIa; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004722; DHOase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR00857; pyrC_multi; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PWS36496.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245765}.
FT DOMAIN 56..422
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 424 AA; 43752 MW; 3EB15E75F9BE0F16 CRC64;
MSLLHITNAR LLDPASGLDA AGELLVRDGI ILDHGTGLGR LDGAEVVDAG GACLAPGLVD
LRAALGEPGA EHRETIASAA QAAAAGGITT LCALPDTDPP LDDAALIQFV IRRGEATGCV
TILPYAAATA GCAGKEIAEY GLLEEAGAVA FTDGTRAIGN ARTMRLALSY ARAFGSFVVQ
HPEEPSLAAG GAATEGERAT RMGLPGIPVA AESMLVARDI ELAKITGGHV HFAHVSTAAA
LAHIRAARVL GLRVTCDTAP PYFDLNETAI GEYRTYAKLS PPLRSDEDRL AVVAALKDGT
IDAIASDHQP RDADDKRLPF AQAEAGGAGL ATLLAVTLAR VHAGDLTLLQ ALDLLTARPA
KLLGIEAGTL RKGAPADLVL FHPERGWRVE AGKLPGKAQN TPFDGRALEG KVLGTWKAGR
RVFG
//
